logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000864_00205

You are here: Home > Sequence: MGYG000000864_00205

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species CAG-632 sp900539185
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-632; CAG-632 sp900539185
CAZyme ID MGYG000000864_00205
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
576 61755.79 4.5397
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000864 2413963 MAG United States North America
Gene Location Start: 212990;  End: 214720  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000864_00205.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 193 379 4.5e-45 0.9943502824858758

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06414 GH25_LytC-like 6.79e-80 192 389 3 191
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599 GH25_muramidase 1.85e-37 192 387 2 185
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
NF033483 PknB_PASTA_kin 3.23e-35 400 535 427 563
Stk1 family PASTA domain-containing Ser/Thr kinase.
NF033483 PknB_PASTA_kin 6.27e-35 398 539 356 499
Stk1 family PASTA domain-containing Ser/Thr kinase.
pfam01183 Glyco_hydro_25 3.54e-32 193 379 1 180
Glycosyl hydrolases family 25.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADL33290.1 4.70e-53 150 389 989 1225
BCK81546.1 4.78e-53 150 389 226 472
AVM48757.1 2.42e-49 174 389 4 214
QHI72152.1 6.24e-48 192 392 95 291
ADK67502.1 1.91e-47 173 387 169 378

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WW5_A 2.29e-17 175 389 250 468
3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A 5.41e-17 175 389 250 468
3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
1JFX_A 1.47e-16 192 386 7 200
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A 7.95e-14 192 386 22 205
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A 3.54e-13 192 386 22 205
X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P25310 2.91e-15 192 386 84 277
Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8FUI5 5.03e-12 398 538 372 514
Probable serine/threonine-protein kinase CE0033 OS=Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) OX=196164 GN=CE0033 PE=3 SV=1
Q8R9T6 5.46e-10 409 535 417 544
Probable serine/threonine-protein kinase Sps1 OS=Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) OX=273068 GN=sps1 PE=3 SV=1
Q8G4G1 8.06e-10 409 498 621 711
Probable serine/threonine-protein kinase pknA2 OS=Bifidobacterium longum (strain NCC 2705) OX=206672 GN=pknA2 PE=3 SV=1
Q9KIG4 9.67e-10 406 538 445 578
Serine/threonine-protein kinase PK-1 OS=Streptomyces toyocaensis OX=55952 GN=spk1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.936462 0.028160 0.001930 0.000225 0.000136 0.033121

TMHMM  Annotations      download full data without filtering help

start end
12 34